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LL-37
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VERIFICATION
How to read this report
LL-37, in structural terms.
- Sequence
- LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES
- Molecular formula
- C₂₀₅H₃₄₀N₆₀O₅₃
- Molecular weight
- 4493 g/mol
- CAS number
- 154947-66-7 — LL-37 (unmodified peptide)This registry number resolves to PubChem CID 16198951, C₂₀₅H₃₄₀N₆₀O₅₃, molecular weight 4493, listed under the synonyms LL-37, cathelicidin LL-37 and ropocamptide. It identifies the unmodified peptide, not an amide or trifluoroacetate salt form. The peptide corresponds to residues 134–170 of the human cathelicidin antimicrobial peptide precursor, UniProt P49913.
- Structure type
- Linear peptide
- Primary molecular target
- Anionic microbial membranes (lipopolysaccharide and lipoteichoic acid); formyl peptide receptor 2 (FPR2/ALX); P2X7 purinergic receptor; Toll-like receptor signalling componentsLL-37 adopts an amphipathic alpha-helical conformation on contact with anionic surfaces. This conformational change is the structural basis of its membrane-interaction behaviour in published in vitro work.
- Physical form
- Lyophilized powder
- PubChem CID
- 16198951
LL-37 continues to be evaluated for its relevance in experimental biology, particularly within studies involving antimicrobial peptide mechanisms, innate immunity, membrane biology, host-defense signaling, inflammatory pathways, and peptide-structure/function relationships.Its 37-amino-acid sequence and cationic, amphipathic characteristics make LL-37 particularly relevant to laboratory investigations examining peptide-membrane interactions and host-defense mechanisms.The peptide is manufactured by solid-phase peptide synthesis.
Where LL-37 appears in the literature.
- Published experimental use of LL-37 includes:
- Membrane permeabilisation and vesicle leakage assays
- Circular dichroism studies of helical transition in anionic environments
- Lipopolysaccharide neutralisation and binding studies
- FPR2/ALX receptor activation assays in cultured cells
- Biofilm formation and disruption studies in bacterial culture
- Structure-activity comparison against truncated fragments such as LL-23, KR-20 and KS-30
- Research use only. Not for human or animal consumption.
- Bacterial culture systems including Gram-positive and Gram-negative strains
- Fungal culture systems
- Model lipid bilayers and supported membranes
- Liposome preparations
- Mammalian cell cultures
- X-ray scattering membrane preparations
- HPLC-UV purity analysis
- LC-MS identity confirmation
- LAL endotoxin assay (USP <85>)
- Minimum inhibitory concentration determination
- Membrane permeabilisation assays
- Circular dichroism secondary structure analysis
- Grazing incidence X-ray diffraction of lipid monolayers
- Calcium flux measurement
- Chromatographic purity
- Peptide identity
- Net peptide content
- Endotoxin assay result
- Minimum inhibitory concentration
- Membrane permeabilisation
- Secondary structure content
- Lipid bilayer ordering
What has been studied, and in what systems.
In preclinical and laboratory research models, LL-37 has been investigated across microbiological, immunological, biochemical, and cellular systems. Research areas include:
Host-defense peptide biology
Microbial membrane interactions
Innate immune signaling
Leukocyte and immune-cell signaling
Cytokine-associated pathways
Epithelial cell biology
Endotoxin interactions
Cellular membrane models
Tissue-repair and re-epithelialization pathways
LL-37’s positive charge and amphipathic structure contribute to its interactions with negatively charged microbial membrane components. Research has also examined functions extending beyond direct antimicrobial activity, including immune-cell signaling and epithelial responses.
These observations are limited to controlled experimental environments and support ongoing laboratory investigation.
These are published research systems. They do not describe approved clinical applications, and they do not establish efficacy or safety in humans.
Chen X et al., 2023. Antimicrobial peptide LL-37 disrupts plasma membrane and calcium homeostasis in Candida albicans via the Rim101 pathway. Microbiol Spectr. PMID 37888991. https://pubmed.ncbi.nlm.nih.gov/37888991/
Martynowycz MW et al., 2019. Salmonella Membrane Structural Remodeling Increases Resistance to Antimicrobial Peptide LL-37. ACS Infect Dis. PMID 31184855. https://pubmed.ncbi.nlm.nih.gov/31184855/
About this compound and its batch data.
What purity did this LL-37 batch achieve?
Lot 2L5 was analysed by Freedom Diagnostics and returned chromatographic purity of 99.83% by HPLC with UV detection coupled to mass spectrometry. Identity was confirmed by mass spectral match. The full certificate is published on this page, and every figure shown here is taken from it.
How much LL-37 is in the vial?
The laboratory measured 6.03 mg, which is 120.6% of the label claim. Net content is reported on a per-vial basis. Astramide publishes the measured figure rather than the label claim, whether it falls above or below.
Was this LL-37 batch tested for endotoxins?
Yes. Endotoxin testing was performed using the Limulus Amebocyte Lysate assay in accordance with USP <85>, and this batch returned Pass, 2 of 2 at ≤0.05 EU/mL. The result appears on the certificate published on this page.
How should LL-37 be stored for research use?
As supplied, the lyophilized powder should be held at -20°C and protected from light and moisture. Once reconstituted, store at 2-8°C and use within 14 to 30 days. Avoid repeated freeze-thaw cycles and follow the handling procedures appropriate to your laboratory.
What is the difference between research-grade and pharmaceutical-grade LL-37?
These are separate classifications. Research-grade material is supplied for laboratory research use only and is not intended for human or animal consumption. Pharmaceutical-grade is an FDA classification that applies to drugs manufactured for human use. Astramide supplies research-grade material only.
How can I verify this LL-37 certificate independently?
The certificate was issued by Freedom Diagnostics under lot 2L5, laboratory reference 2606080490. Quote that reference to the laboratory directly. The same document is published here in full, and is not summarised or reformatted by Astramide.
This product is intended strictly for in-vitro laboratory research conducted by qualified professionals. It is not intended for human or animal consumption, clinical use, or therapeutic application. The statements on this page have not been reviewed by the FDA. These research peptides are not intended to diagnose, treat, cure, or prevent any disease. Research Use Only.








